Trypsin is a serine protease that contains serine, histidine, and aspartic acid residues. Trypsin catalyzes peptide bond hydrolysis through acid catalysis, base catalysis, and covalent catalysis. In the first step serine acts as a nucleophile to attack the substrate peptide bond, which forms a tetrahedral intermediate via covalent catalysis. Then a acyl-enzyme intermediate is formed and the C-terminal fragment is released. A water molecule attacks the acyl enzyme leading to the creation of a second tetrahedral intermediate. This is followed by the release of the N-terminal fragment, which results in the creation of the active enzyme.
Scene 1:catalytic triad . A group of three amino acids that are found in the active site of trypsin: Asp 102, His 57, Ser 195.
Scene 2:acyl intermediate .Formed by the release of the C-terminal fragment from the tetrahedral intermediate.
Scene 3: oxyanion hole . This scene shows the oxyanion hole between Ser 195 and Gly 193, which is an important part of the stabilization of the tetrahedral intermediate. The oxyanion hole is formed between the hydrogen atoms of the amide groups in these two residues.
Scene 4: specificity pocket [1]. The Asp 189 interacts with the Gly 216, which is driven by the specificity of this pocket.
BY: MICHAEL GREEN AND AARON BECKER AND BEIDOU CHENG
[2]
Function
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group.
